|Title||An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Pandit, A., M. Reus, T. Morosinotto, R. Bassi, A.R. Holzwarth, H.J.M. de Groot|
|Journal||Biochimica Et Biophysica Acta-Bioenergetics|
|Keywords||chlamydomonas-reinhardtii, conformational switch, crystal-structure, energy-dissipation, excess energy, excitation-energy, excitonic interactions, major light-harvesting complex ii, non-photochemical quenching, oxygenic photosynthesis, photosynthetic light-harvesting, photosystem-ii, swiss-model, thermal dissipation|
To protect the photosynthetic apparatus against photo-damage in high sunlight, the photosynthetic antenna of oxygenic organisms can switch from a light-harvesting to a photoprotective mode through the process of non-photochemical quenching (NPQ). There is growing evidence that light-harvesting proteins of photosystem II participate in photoprotection by a built-in capacity to switch their conformation between light-harvesting and energy-dissipating states. Here we applied high-resolution Magic-Angle Spinning Nuclear Magnetic Resonance on uniformly C-13-enriched major light-harvesting complex II (LHCII) of Chlamydomonas reinhardtii in active or quenched states. Our results reveal that the switch into a dissipative state is accompanied by subtle changes in the chlorophyll (Chl) a ground-state electronic structures that affect their NMR responses, particularly for the macrocycle (13)C4, (13)C5 and (13)C6 carbon atoms. Inspection of the LHCII X-ray structures shows that of the Chl molecules in the terminal emitter domain, where excited-state energy accumulates prior to further transfer or dissipation, the C4, 5 and 6 atoms are in closest proximity to lutein; supporting quenching mechanisms that involve altered Chl-lutein interactions in the dissipative state. In addition the observed changes could represent altered interactions between Chla and neoxanthin, which alters its configuration under NPQ conditions. The Chls appear to have increased dynamics in unquenched, detergent-solubilized LHCII. Our work demonstrates that solid-state Nuclear Magnetic Resonance is applicable to investigate high-resolution structural details of light-harvesting proteins in varied functional conditions, and represents a valuable tool to address their molecular plasticity associated with photoprotection. (c) 2013 Elsevier B.V. All rights reserved.
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